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• W2509453160 abstract "Protein-surface and protein-crystal interactions are important in many areas of technology including drug and nutraceutical delivery, as many bioactives are highly hydrophobic and tend to crystallize, resulting in poor bioavailability. The improved ability to control lipophilic bioactive nanocrystal formation and dispersibility can increase colloidal stability, and open new ways to control the release of incorporated bioactives and their bioavailability. Herein we compared three model proteins: β-casein, hydrophobin, and β-lactoglobulin, representing different structural groups of proteins, and assessed their functionality in preventing crystal growth, using genistein as a model hydrophobic crystallizing bioactive. Dynamic light scattering, polarized light microscopy and cryo-TEM showed that β-lactoglobulin, hydrophobin and β-casein, respectively inhibit genistein crystal growth in aqueous solution in increasing order of efficacy. Protein structure determines the mechanism and the efficacy by which it affects crystal growth and morphology: β-lactoglobulin, a rigid globular protein with an inward facing hydrophobic domain, indirectly suppresses crystallization by binding and reducing concentration of free hydrophobic compound molecules. Hydrophobin, a rigid globular protein with a flat external hydrophobic domain, adheres to the surface of certain crystal faces, limiting growth in the perpendicular directions. β-casein, a rheomorphic protein with an external hydrophobic domain, adheres to different crystal faces nonspecifically, thereby blocking growth in all directions. Consequently, an inverse correlation was observed between nanocrystal size and in vitro bioavailability. Based on this study, amphiphilic proteins can be more effectively selected and applied to control crystal growth and morphology of hydrophobic bioactives to improve their delivery and bioavailability in food and drug systems." @default.
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• W2509453160 date "2017-02-01" @default.
• W2509453160 modified "2023-09-23" @default.
• W2509453160 title "Harnessing proteins to control crystal size and morphology, for improved delivery performance of hydrophobic bioactives, using genistein as a model" @default.
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• W2509453160 doi "https://doi.org/10.1016/j.foodhyd.2016.08.026" @default.
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